ID A0A0M9YXF7_9ACTN Unreviewed; 442 AA.
AC A0A0M9YXF7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=ADK57_06275 {ECO:0000313|EMBL:KOU75980.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU75980.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOU75980.1}.
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DR EMBL; LGDG01000028; KOU75980.1; -; Genomic_DNA.
DR RefSeq; WP_053748336.1; NZ_LGDG01000028.1.
DR AlphaFoldDB; A0A0M9YXF7; -.
DR STRING; 1415546.ADK57_06275; -.
DR PATRIC; fig|1415546.3.peg.1376; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:KOU75980.1}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..442
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005841947"
FT DOMAIN 27..330
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 337..442
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 442 AA; 46300 MW; 84E6B4A0357EFEC9 CRC64;
MVTRTSIRLG MASLLAIAGL TALSAPADAA STLGAAAAEK GRYFGAAVAA NHLGESAYVS
TLDTEFNSVT PENEMKWDAV ESTRNSFNFT AADQIVSHAQ SKGMKVRGHT LVWHSQLPSW
VGTLAAADLR TAMNNHINQV MGHYKGKIHS WDVVNEAFQD GSSGARRSSP FQDKLGNGFI
EEAFRTARAA DPAAKLCYND YNTDGVNAKS TAVYNLVKDF KARGVPIDCV GFQSHFNSAS
PVPSDYQANL QRFADLGVDV QITELDIEGS GTSQATSYSN VVKACLAVSR CTGITVWGVT
DKYSWRAGGT PLLFDGNYSK KAAYTAVLTA LGGTGSGGGG TAACSVSYSK QEEWSDRFNG
KVTVTAGGSA ISNWTTTVTV TSPQKISATW NGTPTWDSSG NVMTMKPNGN GSLAAGASTS
FGFTVMTNGN TAAPVLGSCT AS
//